Os06g0644200
OVP1 is a member of V-PPases genes in rice[1].
Contents
Annotated Information
Function
OVP1 enhanced cold tolerance is related to cell membrane integrity. The increased protection of membrane integrity was one of key factors for the OVP1 enhanced cold tolerance. V-PPase was an important element in the survival strategies of plants under cold stress[1].
GO assignment(s): GO:0004427,GO:0009678, GO:0015992, GO:0016020
Mutation
OVP1 transgenic rice lines[1]：
- The expression of OVP1 transcript was higher in transgenic rice lines than that in wild type seedlings. The OVP1 transcript levels increased 25.37-fold and 76.02-fold in transgenic lines OE-1 and OE-2, respectively. transgenic lines had 24% and 81% of increased levels of the enzymatic activity respectively as compared to the control plants.
- After cold treatment for 10 days, the survival rates of OVP1 transgenic lines OE-1 and OE-2 were 44.6% and 55.2% respectively, while the survival rate of wild type rice under the same conditions was only 20.2%.
Expression
- Quantitative reverse transcriptase-polymerase chain reaction analysis showed that OVP1 was induced by cold stress. OVP1 overexpression resulted in enhanced cold tolerance in transgenic rice, which was related to an increased integrity of cell membrane, decreased MDA content and accumulation of proline to higher level as compared with wild type rice seedlings. The expression profiling of OVP1 transcript suggested its role in plant tolerance to cold stress with specific regulation mechanisms[1].
- OVP1 expression was also induced by anoxia and chilling stress[1][2]. Northern analysis indicates that the OVPI and OVP2 are also expressed in intact rice plants and OVP2 shows higher expression in the calli than the roots and shoots, compared to OVPI[3] .
Evolution
Figure 1. Phylogenic analysis of deduced amino acid sequences of rice V-PPases.(from reference [4]).
- The relationship between the six V-PPases is shown in a phylogenic tree. The vacuolar H(+)-pyrophosphatase (V-PPase) is an electrogenic H+ pump, which was found in the plant vacuolar membrane[4].
- The sequence analysis has revealed that OVP1 contains 2316 nucleotides of open reading frame (ORF) and 362 nucleotides of the 3'-untranslated region, whereas OVP2 comprises 2304 nucleotides of ORF and 312 nucleotides of the 3'-untranslated region. The nucleotide sequences of ORF of OVPI and OVP2 are 80.7% identical, and their 5'- and 3'-untranslated regions have 39.4% and 48.4% identity, respectively. The polypeptides encoded by the ORF of OVPI and OVP2 contain 771 and 767 amino acids, respectively, and the sequences of the OVP proteins are very similar to those of other V-PPases, which are shown to have 85-91% homology[3].
Knowledge Extension
The vacuolar H+-pyrophosphatase (V-PPase) is an electrogenic H + pump, which was found in the plant vacuolar membrane. In plant cells, H + pumps play important roles in metabolism, homeostasis and regulation of turgot pressure by establishing transmembrane electrochemical gradients which drive translocations of various solutes such as ions, amino acids and sugars across cellular membranes[3].
Labs working on this gene
- State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100094, China
- Molecular Function Laboratory, National Food Research Institute, 2-1-2 Kannondai, Tsukuba, Ibaraki, 305 Japan
- Present address: Department of Applied Physiolog3, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Z~'ukuba, lbaraki, 305 Japan (*author for correspondence)
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Zhang J, Li J, Wang X, et al. OVP1, a vacuolar H+-translocating inorganic pyrophosphatase (V-PPase), overexpression improved rice cold tolerance[J]. Plant Physiology and Biochemistry, 2011, 49(1): 33-38.
- ↑ G.D. Carystinos, H.R. MacDonald, A.F. Monroy, R.S. Dhindsa, R.J. Poole, Vacuolar H(þ)-translocating pyrophosphatase is induced by anoxia or chilling in seedlings of rice, Plant Physiol. 108 (1995) 641e649.
- ↑ 3.0 3.1 3.2 Sakakibara Y, Kobayashi H, Kasamo K. Isolation and characterization of cDNAs encoding vacuolar H+-pyrophosphatase isoforms from rice (Oryza sativa L.)[J]. Plant molecular biology, 1996, 31(5): 1029-1038.
- ↑ 4.0 4.1 Muto Y, Segami S, Hayashi H, et al. Vacuolar proton pumps and aquaporins involved in rapid internode elongation of deepwater rice[J]. Bioscience, biotechnology, and biochemistry, 2011, 75(1): 114-122.
